Crystallization and preliminary X-ray diffraction studies of an RNA aptamer in complex with the human IgG Fc fragment.
Aptamers, which are folded DNA or RNA molecules, bind to target molecules with high affinity and specificity. An RNA aptamer specific for the Fc fragment of human immunoglobulin G (IgG) has recently been identified and it has been demonstrated that an optimized 24-nucleotide RNA aptamer binds to the Fc fragment of human IgG and not to other species. In order to clarify the structural basis of the high specificity of the RNA aptamer, it was crystallized in complex with the Fc fragment of human IgG1. Preliminary X-ray diffraction studies revealed that the crystals belonged to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 83.7, b = 107.2, c = 79.0 A. A data set has been collected to 2.2 A resolution.
Sugiyama
Shigeru
S
Graduate School of Engineering, Osaka University, Suita, Osaka 565-0871, Japan.
Nomura
Yusuke
Y
Sakamoto
Taiichi
T
Kitatani
Tomoya
T
Kobayashi
Asako
A
Miyakawa
Shin
S
Takahashi
Yoshinori
Y
Adachi
Hiroaki
H
Takano
Kazufumi
K
Murakami
Satoshi
S
Inoue
Tsuyoshi
T
Mori
Yusuke
Y
Nakamura
Yoshikazu
Y
Matsumura
Hiroyoshi
H
D001483:Base Sequence; D003461:Crystallography / Q000379:methods; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D007074:Immunoglobulin G / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D009690:Nucleic Acid Conformation; D012313:RNA / Q000737:chemistry / Q000235:genetics* / Q000276:immunology / Q000302:isolation & purification
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D012313:RNA